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P08515

- GST26_SCHJA

UniProt

P08515 - GST26_SCHJA

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Protein

Glutathione S-transferase class-mu 26 kDa isozyme

Gene
N/A
Organism
Schistosoma japonicum (Blood fluke)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate Inferred

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase class-mu 26 kDa isozyme (EC:2.5.1.18)
Short name:
GST 26
Alternative name(s):
Sj26 antigen
SjGST
OrganismiSchistosoma japonicum (Blood fluke)
Taxonomic identifieri6182 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 218217Glutathione S-transferase class-mu 26 kDa isozymePRO_0000185805Add
BLAST

Proteomic databases

PRIDEiP08515.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi6182.P08515.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118
Helixi12 – 143
Helixi15 – 2410
Beta strandi29 – 335
Helixi35 – 373
Helixi38 – 447
Turni45 – 473
Beta strandi55 – 595
Beta strandi64 – 674
Helixi68 – 7811
Helixi86 – 11025
Helixi115 – 13622
Turni137 – 1393
Beta strandi145 – 1473
Helixi150 – 16516
Turni167 – 1726
Helixi174 – 18512
Helixi187 – 1937
Beta strandi195 – 1973
Beta strandi203 – 2075
Beta strandi209 – 2113
Beta strandi213 – 2153

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B8XX-ray2.70A2-218[»]
1BG5X-ray2.60A1-218[»]
1DUGX-ray1.80A/B2-218[»]
1GNEX-ray2.50A2-218[»]
1GTAX-ray2.40A1-218[»]
1GTBX-ray2.60A1-218[»]
1M99X-ray2.30A1-218[»]
1M9AX-ray2.10A1-218[»]
1M9BX-ray2.60A1-218[»]
1U87X-ray3.50A1-218[»]
1U88X-ray3.50A/B1-218[»]
1UA5X-ray2.50A1-218[»]
1Y6EX-ray3.00A/B2-218[»]
3CRTX-ray1.90A1-214[»]
3CRUX-ray2.30A1-214[»]
3D0ZX-ray2.50A1-214[»]
3QMZX-ray6.00S/T2-218[»]
4AI6X-ray3.40A/B2-218[»]
4AKGX-ray3.30A/B2-218[»]
4AKHX-ray3.60A/B2-218[»]
4AKIX-ray3.70A/B2-218[»]
4ECBX-ray2.20A/B1-218[»]
4ECCX-ray2.20A1-215[»]
ProteinModelPortaliP08515.
SMRiP08515. Positions 2-218.

Miscellaneous databases

EvolutionaryTraceiP08515.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GST N-terminalAdd
BLAST
Domaini85 – 203119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione binding
Regioni41 – 455Glutathione binding
Regioni54 – 552Glutathione binding
Regioni67 – 682Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.

Phylogenomic databases

eggNOGiNOG300089.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08515-1 [UniParc]FASTAAdd to Basket

« Hide

MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL    50
EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL 100
DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH 150
PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA 200
WPLQGWQATF GGGDHPPK 218
Length:218
Mass (Da):25,499
Last modified:January 23, 2007 - v3
Checksum:i5E2AC418BD0EF13F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14654 mRNA. Translation: AAB59203.1.
PIRiA61514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14654 mRNA. Translation: AAB59203.1 .
PIRi A61514.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B8X X-ray 2.70 A 2-218 [» ]
1BG5 X-ray 2.60 A 1-218 [» ]
1DUG X-ray 1.80 A/B 2-218 [» ]
1GNE X-ray 2.50 A 2-218 [» ]
1GTA X-ray 2.40 A 1-218 [» ]
1GTB X-ray 2.60 A 1-218 [» ]
1M99 X-ray 2.30 A 1-218 [» ]
1M9A X-ray 2.10 A 1-218 [» ]
1M9B X-ray 2.60 A 1-218 [» ]
1U87 X-ray 3.50 A 1-218 [» ]
1U88 X-ray 3.50 A/B 1-218 [» ]
1UA5 X-ray 2.50 A 1-218 [» ]
1Y6E X-ray 3.00 A/B 2-218 [» ]
3CRT X-ray 1.90 A 1-214 [» ]
3CRU X-ray 2.30 A 1-214 [» ]
3D0Z X-ray 2.50 A 1-214 [» ]
3QMZ X-ray 6.00 S/T 2-218 [» ]
4AI6 X-ray 3.40 A/B 2-218 [» ]
4AKG X-ray 3.30 A/B 2-218 [» ]
4AKH X-ray 3.60 A/B 2-218 [» ]
4AKI X-ray 3.70 A/B 2-218 [» ]
4ECB X-ray 2.20 A/B 1-218 [» ]
4ECC X-ray 2.20 A 1-215 [» ]
ProteinModelPortali P08515.
SMRi P08515. Positions 2-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 6182.P08515.

Chemistry

DrugBanki DB00143. Glutathione.
DB01058. Praziquantel.

Proteomic databases

PRIDEi P08515.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG300089.

Miscellaneous databases

EvolutionaryTracei P08515.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase."
    Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.
    Proc. Natl. Acad. Sci. U.S.A. 83:8703-8707(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.
    Proc. Natl. Acad. Sci. U.S.A. 84:6541-6541(1987)
    Cited for: SEQUENCE REVISION.
  3. "Expression of an enzymatically active parasite molecule in Escherichia coli: Schistosoma japonicum glutathione S-transferase."
    Smith D.B., Rubira M.R., Simpson R.J., Davern K.M., Tiu W.U., Board P.G., Mitchell G.F.
    Mol. Biochem. Parasitol. 27:249-256(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15.
  4. "Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV."
    Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Ruker F., Carter D.C.
    Protein Sci. 3:2233-2244(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  5. "Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel."
    McTigue M.A., Williams D.R., Tainer J.A.
    J. Mol. Biol. 246:21-27(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITOR PRAZIQUANTEL.
  6. "Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum."
    Cardoso R.M., Daniels D.S., Bruns C.M., Tainer J.A.
    Proteins 51:137-146(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE ANALOGS.
  7. "Using affinity chromatography to engineer and characterize pH-dependent protein switches."
    Sagermann M., Chapleau R.R., DeLorimier E., Lei M.
    Protein Sci. 18:217-228(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-214.

Entry informationi

Entry nameiGST26_SCHJA
AccessioniPrimary (citable) accession number: P08515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

There are at least two isoenzymes of GST in S.japonicum.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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